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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
(S)-6-hydroxynicotine + H2O + O2
6-hydroxy-pseudooxynicotine + H2O2
(S)-6-hydroxynornicotine + H2O + O2
?
-
-
-
-
?
(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
2-phenylethylamine + H2O + O2
2-phenylethanal + NH3 + H2O2
-
-
-
-
?
6-hydroxy-L-nicotine + H2O + O2
6-hydroxy-N-methylmyosmine + NH3 + H2O2
-
-
-
-
?
benzylamine + H2O + O2
benzaldehyde + NH3 + H2O2
-
-
-
-
?
L-6-hydroxy-nor-nicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-aminobutan-1-one + H2O2
-
-
-
-
?
nicotine + H2O + O2
N-methylmyosmine + H2O2
-
-
-
?
additional information
?
-
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is involved in degradation of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
absolute stereospecificity on the L-form
intermediate product 6-hydroxy-N-methylmyosmine, which hydrolyzes to 6-hydroxy-pseudooxynicotine
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is essential for nicotine or (S)-6-hydroxynicotine degradation
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme converts (S)-6-hydroxynicotine into 6-hydroxy-N-methylmyosmine which then spontaneously hydrolyzes into 6-hydroxypseudooxynicotine. (S)-6-Hydroxynicotine is the preferred substrate in vivo. The enzyme shows no activities toward the R enantiomer of nicotine or 6-hydroxynicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
6-hydroxy-pseudooxynicotine + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
6-hydroxy-pseudooxynicotine + H2O2
-
-
-
-
?
(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
-
-
-
?
(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
N-methyl-myosmine, which is nonenzymatically hydrolyzed to pseudooxynicotine. The flavoenzyme preferentially oxidizes tertiary amines with an efficient reductive half-reaction and a very slow oxidative half-reaction when O2 is the oxidizing substrate, suggesting that the true oxidizing agent is unknown
-
-
?
(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
N-methyl-myosmine, which is nonenzymatically hydrolyzed to pseudooxynicotine. The flavoenzyme preferentially oxidizes tertiary amines with an efficient reductive half-reaction and a very slow oxidative half-reaction when O2 is the oxidizing substrate, suggesting that the true oxidizing agent is unknown
-
-
?
(S)-nicotine + H2O + O2
N-methylmyosmine + H2O2
the enzyme converts (S)-nicotine into N-methylmyosmine, which spontaneously hydrolyzes into pseudooxynicotine
-
-
?
additional information
?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
measurement of enzyme activity using dichlorindophenol. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
-
-
?
additional information
?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
measurement of enzyme activity using dichlorindophenol. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
-
-
?
additional information
?
-
-
also oxidizes circular secondary and tertiary amines
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
it is synthesized only during the logarithmic and stationary phases of growth
-
-
?
additional information
?
-
-
no activity with 6-hydroxy-D-nicotine
-
-
?
additional information
?
-
-
synthesis of 6-hydroxy-N-methylmyosmine and 6-hydroxy-pseudooxynicotine from 6-hydroxy-L-nicotine. 6-Hydroxypseudooxynicotine forms from 6-hydroxy-N-methylmyosmine non-enzymatically
-
-
?
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(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
6-hydroxy-L-nicotine + H2O + O2
6-hydroxy-N-methylmyosmine + NH3 + H2O2
-
-
-
-
?
additional information
?
-
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyrid-3-yl)-4-(methylamino)-butan-1-one + H2O2
-
-
transitional product is 6-hydroxy-N-methylmyosmine that hydrolyses spontaneously
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
-
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is involved in degradation of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
absolute stereospecificity on the L-form
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
-
-
?
(S)-6-hydroxynicotine + H2O + O2
1-(6-hydroxypyridin-3-yl)-4-(methylamino)butan-1-one + H2O2
the enzyme is essential for nicotine or (S)-6-hydroxynicotine degradation
-
-
?
additional information
?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
transformation of 6-hydroxy-L-nicotine to 6-hydroxy-N-methylmyosmine, 6-hydroxypseudooxynicotine formation, overview
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
enzyme production is induced by growing cells in D,L-nicotine as only source of carbon and nitrogen
-
-
?
additional information
?
-
-
it is synthesized only during the logarithmic and stationary phases of growth
-
-
?
additional information
?
-
-
no activity with 6-hydroxy-D-nicotine
-
-
?
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9.26 - 1020
(S)-6-hydroxynicotine
2 - 370
(S)-6-hydroxynornicotine
0.0076 - 0.195
(S)-nicotine
9.26
(S)-6-hydroxynicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
14
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme N166A
24
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme K287M
26.5
(S)-6-hydroxynicotine
mutant Y311W, pH 7.4, 22°C
103
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
379
(S)-6-hydroxynicotine
pH 7.0, 40°C
600
(S)-6-hydroxynicotine
-
pH 7.0, 25°C, wild-type enzyme
1020
(S)-6-hydroxynicotine
wild-type, pH 7.4, 22°C
2
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, mutant enzyme N166A
8.6
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, mutant enzyme Y311F
370
(S)-6-hydroxynornicotine
-
pH 7.0, 25°C, wild-type enzyme
0.0076
(S)-nicotine
mutant Y311W, pH 7.4, 22°C
0.0077
(S)-nicotine
wild-type, pH 7.4, 22°C
0.0204
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 22°C
0.0877
(S)-nicotine
mutant R274A/Y311W/C417W, pH 7.4, 37°C
0.195
(S)-nicotine
pH 7.0, 40°C
0.018
Nicotine
37°C, pH not specified in the publication
0.024
Nicotine
37°C, pH not specified in the publication
0.048
O2
-
pH 7.0, 25°C, mutant enzyme K287M, cosubstrate: (S)-6-hydroxynicotine
24
O2
-
pH 7.0, 25°C, mutant enzyme N166A, cosubstrate: (S)-6-hydroxynicotine
110
O2
-
pH 7.0, 25°C, mutant enzyme Y311F, cosubstrate: (S)-6-hydroxynicotine
150
O2
-
pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynornicotine
270
O2
-
pH 7.0, 25°C, wild-type enzyme, cosubstrate: (S)-6-hydroxynicotine
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evolution
-
enzyme is part of a nicotine-degrading gene cluster, ndp, containing the nicotine hydroxylase, 6-hydroxy-L-nicotine oxidase, 6-hydroxypseudooxynicotine oxidase, and 6-hydroxy-3-succinyl-pyridine monooxygenase responsible for catalyzing the transformation of nicotine to 2,5-dihydropyridine. The linked ndpHFEG genes shared by the variant of the pyridine and pyrrolidine pathways and pyrrolidine pathways indicate that these two pathways might share the same origin
evolution
-
enzyme is part of a nicotine-degrading gene cluster, ndp, containing the nicotine hydroxylase, 6-hydroxy-L-nicotine oxidase, 6-hydroxypseudooxynicotine oxidase, and 6-hydroxy-3-succinyl-pyridine monooxygenase responsible for catalyzing the transformation of nicotine to 2,5-dihydropyridine. The linked ndpHFEG genes shared by the variant of the pyridine and pyrrolidine pathways and pyrrolidine pathways indicate that these two pathways might share the same origin
-
metabolism
-
pathways of nicotine degradation by bacteria
metabolism
-
the enzyme is involved in nicotine degradation, five hydroxylated-pyridine intermediates during the cell growth on nicotine and during transformation of nicotine within resting cells, overview. Agrobacterium strain S33 employs a novel pathway that is different from the two characterized pathways described in Arthrobacter and Pseudomonas. Agrobacterium strain S33 is able to transform nicotine to 6-hydroxypseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine. The cell extract can transform 6-hydroxypseudooxynicotine into 6-hydroxy-3-succinoylpyridine by coupling with 6-hydroxy-Lnicotine oxidation reaction by 6-hydroxy-L-nicotine oxidase. Pathways of nicotine degradation by bacteria,, overview
metabolism
the deletion and complementation of the nctB gene shows that this enzyme is essential for nicotine or (S)-6-hydroxynicotine degradation
metabolism
-
the enzyme catalyzes the oxidation of (S)-6-hydroxynicotine to 6-hydroxypseudooxynicotine during microbial catabolism of nicotine
metabolism
resiudes Asn166, Tyr311, and Lys287 as well as an active site water molecule have roles in the catalysis of the enzyme. A hydride transfer mechanism is the only viable mechanism for catalysis. During the hydride transfer process an active site water molecule bridges FAD and Lys287 through H-bonding interaction. A series of H-bonding interactions coupled with van der Waals interactions keep FAD and substrate S-6-hydroxynicotine closer. FAD achieves a bent conformation
metabolism
-
the enzyme is involved in nicotine degradation, five hydroxylated-pyridine intermediates during the cell growth on nicotine and during transformation of nicotine within resting cells, overview. Agrobacterium strain S33 employs a novel pathway that is different from the two characterized pathways described in Arthrobacter and Pseudomonas. Agrobacterium strain S33 is able to transform nicotine to 6-hydroxypseudooxynicotine first via the pyridine pathway through 6-hydroxy-L-nicotine and 6-hydroxy-N-methylmyosmine, and then, it turns to the pyrrolidine pathway with the formation of 6-hydroxy-3-succinoylpyridine and 2,5-dihydroxypyridine. The cell extract can transform 6-hydroxypseudooxynicotine into 6-hydroxy-3-succinoylpyridine by coupling with 6-hydroxy-Lnicotine oxidation reaction by 6-hydroxy-L-nicotine oxidase. Pathways of nicotine degradation by bacteria,, overview
-
physiological function
-
expression of the 6-hydroxy-L-nicotine oxidase gene allows the bacterium to take up L-nicotine
physiological function
-
after disruption of ndpB gene, the mutant strain loses the ability to grow on nicotine and accumulates 6-hydroxynicotine
physiological function
-
after disruption of ndpB gene, the mutant strain loses the ability to grow on nicotine and accumulates 6-hydroxynicotine
-
physiological function
-
expression of the 6-hydroxy-L-nicotine oxidase gene allows the bacterium to take up L-nicotine
-
additional information
the flavin may have a role in oxygen activation involving replacement of the water molecule by oxygen and superoxide formation. The orientation of the bound substrate relative to the isoalloxazine ring of the FAD cofactor is suitable for hydride transfer dehydrogenation at the carbon atom that forms the chiral center of the substrate molecule, substrate-binding mode, overview. In the dithionite-reduced 6HLNO, the natural substrate 6-hydroxy-L-nicotine is located in a tight cavity suggesting that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions
additional information
-
the flavin may have a role in oxygen activation involving replacement of the water molecule by oxygen and superoxide formation. The orientation of the bound substrate relative to the isoalloxazine ring of the FAD cofactor is suitable for hydride transfer dehydrogenation at the carbon atom that forms the chiral center of the substrate molecule, substrate-binding mode, overview. In the dithionite-reduced 6HLNO, the natural substrate 6-hydroxy-L-nicotine is located in a tight cavity suggesting that the binding geometry of this unproductive complex may be closely similar as under oxidizing conditions
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D166Q
mutation slightly reduces the KM for nicotine, it also reduced enzyme turnover by 5fold with nicotine
K287M
-
mutation results in an about 10-fold decreases in kcat/Km and k(red) for (S)-6-hydroxynicotine and a 6000-fold decrease in the kcat/Km value for oxygen
N166A
-
mutation results in an about 30fold decrease in kcat/Km and k(red) for (S)-6-hydroxynicotine, respectively, with larger effects on the kcat/Km value for (S)-6-hydroxynornicotine. The shapes of the pH profiles are not altered
R274A/Y311W/C417W
combination of mutations predicted to enhance enzyme stability, and mutation Y311W. The triple mutant displays an increased kcat value for nicotine resulting in a comparatively robust oxidation of (S)-nicotine, at the same time reducing the specificity for (S)-OH-nicotine by more than 100fold and increasing that for (S)-nicotine by more than fold
Y311F
-
mutation results in an about 30fold decrease in kcat/Km and k(red) for (S)-6-hydroxynicotine, respectively, with larger effects on the kcat/Km value for (S)-6-hydroxynornicotine. The shapes of the pH profiles are not altered
Y311W
active site residue Tyr311 forms a hydrogen bond with the hydroxyl group of (S)-6-OH-nicotine within the catalytic pocket. Replacement by a tryptophan residue reduces the kcat for (S)-6-OH-nicotine by more than 6fold
N462H
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
N462Y/W427Y
mutant enzyme shows increased catalytic activity
W427V
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
N462H
-
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
-
N462Y/W427Y
-
mutant enzyme shows increased catalytic activity
-
W427V
-
the variant shows moderately higher oxidase activity, reductive half-reaction using (S)-nicotine is significantly slower than that of wild-type enzyme
-
additional information
adding a maltose-binding protein tag onto the N-terminus markedly increases the thermal stability of the enzyme and increases the observed Vmax value for 6-OH-nicotine by about 4.5fold, due to an increase in the occupancy of the flavin cofactor following expression and purification
additional information
-
adding a maltose-binding protein tag onto the N-terminus markedly increases the thermal stability of the enzyme and increases the observed Vmax value for 6-OH-nicotine by about 4.5fold, due to an increase in the occupancy of the flavin cofactor following expression and purification
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Schenk, S.; Hoelz, A.; Krauss, B.; Decker, K.
Gene structures and properties of enzymes of the plasmid-encoded nicotine catabolism of Arthrobacter nicotinovorans
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Paenarthrobacter nicotinovorans
brenda
Grether-Beck, S.; Igloi, G.L.; Pust, S.; Schilz, E.; Decker, K.; Brandsch, R.
Structural analysis and molybdenum-dependent expression of the pAO1-encoded nicotine dehydrogenase genes of Arthrobacter nicotinovorans
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Paenarthrobacter nicotinovorans
brenda
Pust, S.; Vervoort, J.; Decker, K.; Bacher, A.; Muller, F.
13C, 15N, and 31P NMR studies on 6-hydroxy-L-nicotine oxidase from Arthrobacter oxidans
Biochemistry
28
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1989
Paenarthrobacter nicotinovorans
brenda
Brandsch, R.; Hinkkanen, A.E.; Mauch, L.; Nagursky, H.; Decker, K.
6-Hydroxy-D-nicotine oxidase of Arthrobacter oxidans. Gene structure of the flavoenzyme and its relationship to 6-hydroxy-L-nicotine oxidase
Eur. J. Biochem.
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1987
Paenarthrobacter nicotinovorans
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Swafford, J.R.; Reeves, H.C.; Brandsch, R.
Localization of the enantiozymes of 6-hydroxy-nicotine oxidase in Arthrobacter oxidans by electron immunochemistry
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1985
Paenarthrobacter nicotinovorans
brenda
Hinkkanen, A.; Lilius, E.M.; Nowack, J.; Maas, R.; Decker, K.
Purification of the flavoproteins 6-hydroxy-D- and 6-hydroxy-L-nicotine oxidase using hydrophobic affinity chromatography
Hoppe-Seyler's Z. Physiol. Chem.
364
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1983
Paenarthrobacter nicotinovorans
brenda
Decker, K.; Dai, V.D.; Mhler, H.; Bruhmuller, M.
D- and L-6-hydroxynicotine oxidase, enantioenzymes of Arthrobacter oxidans
Z. Naturforsch. B
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1972
Paenarthrobacter nicotinovorans
brenda
Palmer, G.; Massey, V.
Mechanisms of flavoprotein catalysis
Biol. Oxidations (Singer, T. P. , ed. )
263-300
1968
Paenarthrobacter nicotinovorans
-
brenda
Dai, V.D.; Decker, K.; Sund, H.
Purification and properties of L-6-hydroxynicotine oxidase
Eur. J. Biochem.
4
95-102
1968
Paenarthrobacter nicotinovorans
brenda
Decker, K.; Dai, V.D.
Mechanism and specifcity of L- and D-6-hydroxynicotine oxidase
Eur. J. Biochem.
3
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1967
Paenarthrobacter nicotinovorans
brenda
Decker, K.; Bleeg, H.
Induction and purification of stereospecific nicotine oxidizing enzymes from Arthrobacter oxidans
Biochim. Biophys. Acta
105
313-324
1965
Paenarthrobacter nicotinovorans
brenda
Schenk, S.; Decker, K.
Horizontal gene transfer involved in the convergent evolution of the plasmid-encoded enantioselective 6-hydroxynicotine oxidases
J. Mol. Evol.
48
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1999
Paenarthrobacter nicotinovorans
brenda
Ganas, P.; Brandsch, R.
Uptake of L-nicotine and of 6-hydroxy-L-nicotine by Arthrobacter nicotinovorans and by Escherichia coli is mediated by facilitated diffusion and not by passive diffusion or active transport
Microbiology
155
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2009
Paenarthrobacter nicotinovorans, Paenarthrobacter nicotinovorans PAO1
brenda
Kachalova, G.S.; Bourenkov, G.P.; Mengesdorf, T.; Schenk, S.; Maun, H.R.; Burghammer, M.; Riekel, C.; Decker, K.; Bartunik, H.D.
Crystal structure analysis of free and substrate-bound 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans
J. Mol. Biol.
396
785-799
2010
Paenarthrobacter nicotinovorans (Q93NH4), Paenarthrobacter nicotinovorans
brenda
Wang, S.; Huang, H.; Xie, K.; Xu, P.
Identification of nicotine biotransformation intermediates by Agrobacterium tumefaciens strain S33 suggests a novel nicotine degradation pathway
Appl. Microbiol. Biotechnol.
95
1567-1578
2012
Agrobacterium tumefaciens, Paenarthrobacter nicotinovorans, Agrobacterium tumefaciens S33
brenda
Kachalova, G.; Decker, K.; Holt, A.; Bartunik, H.D.
Crystallographic snapshots of the complete reaction cycle of nicotine degradation by an amine oxidase of the monoamine oxidase (MAO) family
Proc. Natl. Acad. Sci. USA
108
4800-4805
2011
Paenarthrobacter nicotinovorans
brenda
Qiu, J.; Wei, Y.; Ma, Y.; Wen, R.; Wen, Y.; Liu, W.
A novel (S)-6-hydroxynicotine oxidase gene from Shinella sp. strain HZN7
Appl. Environ. Microbiol.
80
5552-5560
2014
Shinella sp. (A0A075BSX9), Shinella sp.
brenda
Yu, H.; Tang, H.; Zhu, X.; Li, Y.; Xu, P.
Molecular mechanism of nicotine degradation by a newly isolated strain, Ochrobactrum sp. strain SJY1
Appl. Environ. Microbiol.
81
272-281
2015
Ochrobactrum sp. SJY1 (A0A075XFI8)
brenda
Fitzpatrick, P.F.; Chadegani, F.; Zhang, S.; Dougherty, V.
Mechanism of flavoprotein L-6-hydroxynicotine oxidase pH and solvent isotope effects and identification of key active site residues
Biochemistry
56
869-875
2017
Paenarthrobacter nicotinovorans
brenda
Deay, D.I.; Colvert, K.; Gao, F.; Seibold, S.; Goyal, P.; Aillon, D.; Petillo, P.; Richter, M.
An active site mutation in 6-hydroxy-L-nicotine oxidase from Arthrobacter nicotinovorans changes the substrate specificity in favor of (S)-nicotine
Arch. Biochem. Biophys.
692
108520
2020
Paenarthrobacter nicotinovorans (Q93NH4), Paenarthrobacter nicotinovorans
brenda
Tararina, M.A.; Dam, K.K.; Dhingra, M.; Janda, K.D.; Palfey, B.A.; Allen, K.N.
Fast kinetics reveals rate-limiting oxidation and the role of the aromatic cage in the mechanism of the nicotine-degrading enzyme NicA2
Biochemistry
60
259-273
2021
Pseudomonas putida (F8G0P2), Pseudomonas putida, Pseudomonas putida S16 (F8G0P2)
brenda
Wang, H.; Zhi, X.; Qiu, J.; Shi, L.; Lu, Z.
Characterization of a novel nicotine degradation gene cluster ndp in Sphingomonas melonis TY and its evolutionary analysis
Front. Microbiol.
8
337
2017
Sphingomonas melonis, Sphingomonas melonis TY
brenda
Yildiz, I.; Yildiz, B.S.
Mechanistic study of L-6-hydroxynicotine oxidase by DFT and ONIOM methods
J. Mol. Model.
27
53
2021
Paenarthrobacter nicotinovorans (Q93NH4)
brenda
Li, J.; Shen, M.; Chen, Z.; Pan, F.; Yang, Y.; Shu, M.; Chen, G.; Jiao, Y.; Zhang, F.; Linhardt, R.; Zhong, W.
Expression and functional identification of two homologous nicotine dehydrogenases, NicA2 and Nox, from Pseudomonas sp. JY-Q
Protein Expr. Purif.
178
105767
2021
Pseudomonas sp. JY-Q, Pseudomonas sp. JY-Q (A0A0S4IEN1)
brenda